The natural world is scoured for genomic products with desired properties for human applications. Artificially, novel RNA and protein functions can be achieved by the use of recombinant DNA technology to generate new biological entities. However, very little has been done to endow unmodified RNAs or proteins with novel biological functions. Artificially-derived antigen-binding proteins such as nanobodies have been used for the inhibition or degradation of intracellular target antigens. The inverse strategy of using artificially-derived antigen binding proteins linked to other molecules that promote enhanced activity of the resulting complex formed by the addition of an intracellular non-native antigen to activate synthetic devices, has apparently never been attempted. Fluorescent proteins are now used to label specific cell types and proteins in a wide range of organisms. The majority of GFP applications exploit GFP fluorescent properties to trace cellular processes such as gene expression and protein localization (Tsien, 1998; Chalfie et al., 1994; Ogawa et al., 1995; Miyawaki et al., 1997; Patterson et al., 2002; Berg et al, 2009). GFP is useful for these instances because it is extraordinarily inert in heterologous systems. It is freely diffusible in the cytoplasm, can enter the nucleus, has low cytotoxicity and few non-specific interactions with host proteins (Ogawa et al., 1995; Trinkle-Mulcahy et al., 2008).